NIU Department of
Chemistry & Biochemistry
Where the study of matter...matters!
Office: La Tourette Hall 326
Phone: (815) 753‐6871
Presidential Young Investigator Award, National Science Foundation, 1991
Research Associate, University of Houston, 1987–1990
Research Associate, Stanford University, 1985–1987
Ph.D., Cornell University, 1986
M.S., Cornell University, 1983
B.S., Sichuan University, 1978
Structure, bonding, and physical properties of solid‐state materials; theoretical study of protein structure and dynamics; electron transfer processes in biological systems.
Eurh‐kamen: Ln‐Oktaedertripel in Ln14(C2)3I20 mit Ln = La, Ce. Mattausch, H.; Simon, A.; Kienle, L.; Hoch, C.; Zheng, C.; Kremer, R. K. (2006) Z. Anorg. Allg. Chem., 632: 1661–1670.
Structure prediction of the RPE65 protein. Guo, H.;Zheng, C.; Gaillard, E. R. (2006) J. Theor. Biol., 242: 117–122.
Shape‐persistent macrocyclic aromatic tetrasul‐fonamides: Molecules with nanosized cavities and their nanotubular assemblies in solid state. He, L.; An, Y.; Yuan, L.; Feng, W.; Li, M.; Zhang, D.; Yamato, K.; Zheng, C.; Zeng, X. C.; Gong, B. (2006) Proc. Natl. Acad. Sci. U.S.A., 103: 10850–10855.
Fused stars and nano‐stripes in the rare earth halide La7Sb11Br4. Zheng, C.; Mattausch, H.; Li, S.‐J. (2005) Z. Anorg. Allg. Chem., 631: 421–426.
La9Sb16Br3 and Ce9Sb16Cl3: Stars and stripes in rare earth halide and intermetallic compounds. Zheng, C.; Mattausch, H.; Simon, A. (2005) Inorg. Chem., 44: 3684–3689.
La4Br2Al5 and Ce4Br2Al5: Three‐dimensional metal networks embedded in fused Ln6trigonal prisms. Zheng, C.; Mattausch, H.; Oeckler, O.; Nuss, J.; Simon, A. (2003) Z. Anorg. Allg. Chem., 629: 2229–2235.
Ce10Cl4Ga5 and Ln3ClGa4 (Ln = La, Ce): Reduced halides or oxidized intermetallics?Zheng, C.; Mattausch, H.; Oeckler, O.; Simon, A. (2003) Inorg. Chem., 42: 3130–3135.
Porous lanthanide‐organic frameworks: Synthesis, characterization, and unprecedented gas adsorption properties. Pan, L.; Adams, K. M.; Hernandez, H. E.; Wang, X.; Zheng, C.; Hattori, Y.; Kaneko, K. (2003) J. Am. Chem. Soc., 125: 3062–3067.
Materials science has seen rapid development in the last decade. Superconductors, nanostructures, and self‐assembly systems, for example, are several of the many fruits of research into this field. Our research focuses on one aspect of materials science, specifically solid‐state materials with novel physical, chemical, or biological properties. Our scientific endeavor consists of both experimental and theoretical work. In the experimental portion of our research, we look for and analyze potentially magnetic or superconducting materials using solid‐state chemical techniques. We are interested, among other things, in how the electronic structures of solids can affect their chemical bonding behavior, and how that bonding behavior will determine their physical properties. Tools we use in this research include high‐temperature synthesis, powder and single crystal X‐ray diffraction, and measurements of physical properties.
In the theoretical part of our research, we analyze the electronic structure of solids, simulate the chemical reaction process in the solid state, and compare the results of our theoretical models with experimental observations. Through the interplay of experimentation and theoretical analysis, we hope to find better ways of making solid state materials with desired chemical and physical properties.
Localized electron density in the solid‐state compound BaAl4.
Our theoretical component also includes computer modeling and simulation of biological systems. We try to understand how structures and dynamics can affect the biological functions and behaviors of proteins and lipids. Heme proteins are currently our main interest in this research, and the primary tool we use is a high‐speed computer equipped with powerful interactive graphics.
We are also interested in electron and proton transfer processes in biological systems. Computer simulation of these transfer processes requires more sophisticated theoretical techniques because of the quantum nature of electrons and protons. The Feynman path integral method is usually used. Using a fast computer to arrive at numerical solutions of the quantum mechanical equation, we can study how electron and proton transfer processes are affected by the protein environment.